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Characterization of lipid binding specificities of dysferlin C2 domains reveals novel interactions with phosphoinositides

Therrien, Christian and Di Fulvio, Sabrina and Pickles, Sarah and Sinnreich, Michael. (2009) Characterization of lipid binding specificities of dysferlin C2 domains reveals novel interactions with phosphoinositides. Biochemistry : a biweekly publication of the American Chemical Society, Vol. 48. pp. 2377-2384.

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Official URL: http://edoc.unibas.ch/dok/A6003606

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Abstract

Dysferlin is a type II transmembrane protein implicated in Ca(2+)-dependent sarcolemmal membrane repair. Dysferlin has seven C2 domains, which are lipid and protein binding modules. In this study, we sought to characterize the lipid binding specificity of dysferlin's seven C2 domains. Dysferlin's C2A domain was able to bind to phosphatidylserine (PS), phosphatidylinositol 4-phosphate [PtdIns(4)P], and phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P(2)] in a Ca(2+)-dependent fashion. The remainder of the C2 domains exhibited weaker and Ca(2+)-independent binding to PS and no significant binding to phosphoinositides.
Faculties and Departments:03 Faculty of Medicine > Departement Biomedizin > Department of Biomedicine, University Hospital Basel > Neuromuscular Research (Sinnreich)
UniBasel Contributors:Sinnreich, Michael
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Chemical Society
ISSN:0006-2960
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:24 May 2013 09:21
Deposited On:24 May 2013 08:59

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